In recent years, our understanding of protein structure and function has advanced rapidly,
providing a mechanistic understanding of a wide variety of biological processes. As an …

The construction of complex protein folds relies on the precise conversion of a linear
polypeptide chain into a compact 3-dimensional structure. The interplay of forces that link …

The remarkable complexity of globular protein structures was first revealed about half a
century ago, when the crystal structure of myoglobin was determined at 2.4 Å. 1 In the …

Enantiomerically pure β‐amino‐acid derivatives with the side chains of Ala, Val, and Leu in
the 2‐or 3‐position (β2‐and β3‐amino acids, resp.), as well as with substituents in both the 2 …

The secondary structures of oligomeric organic molecules are known to reveal fascinating
architectures that can be responsible for their aesthetic beauty as well as their biological …

Recently, it has been discovered that peptides composed of β‐amino acids are capable of
adopting novel secondary structures demonstrating that peptides composed of α‐amino …

Interplay between proteins, nucleic acids, carbohydrates and/or lipids is involved in almost
every process in life on earth. As a consequence, a wide range of diseases results from …

α, γ-and β, γ-hybrid peptides, which are composed of two different homologous amino acid
constituents in alternate order, are suggested as novel classes of peptide foldamers. On the …

As one of the most important families of non‐natural polymers with the propensity to form
well‐defined secondary structures, the β‐peptides are attracting increasing attention. The …

Two N-terminally protected dipeptides with a β-amino acid residue form hydrogels at
physiological pH and temperature. These two hydrogels have been characterized by various …